메뉴 건너뛰기




Volumn 388, Issue 2, 2005, Pages 679-687

Evidence for the occurrence of membrane-type serine protease 1/matriptase on the basolateral sides of enterocytes

Author keywords

Cell cell and or cell substratum adhesion; Enterocyte; MT SP1 matriptase; N terminal fragment; Small intestine epithelial cell; Subcellular distribution

Indexed keywords

ADHESION; CELL MEMBRANES; CELLS; ENZYME INHIBITION; FRACTIONATION; MOLECULES;

EID: 20544441281     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041639     Document Type: Article
Times cited : (39)

References (34)
  • 1
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • Albelda, S. M. and Buck, C. A. (1990) Integrins and other cell adhesion molecules. FASEB J. 4, 2868-2880
    • (1990) FASEB J. , vol.4 , pp. 2868-2880
    • Albelda, S.M.1    Buck, C.A.2
  • 2
    • 0000798128 scopus 로고
    • The functional morphology of the mucosa of the small intestine
    • (Johnson, L. R., ed.), Raven Press, New York, NY
    • Madara, J. L. and Trier, J. S. (1994) The functional morphology of the mucosa of the small intestine. In Physiology of the Gastrointestinal Tract, 3rd edn. (Johnson, L. R., ed.), pp. 1577-1622, Raven Press, New York, NY
    • (1994) Physiology of the Gastrointestinal Tract, 3rd Edn. , pp. 1577-1622
    • Madara, J.L.1    Trier, J.S.2
  • 3
    • 0030472432 scopus 로고    scopus 로고
    • Apoptosis and gastrointestinal pharmacology
    • Pritchard, M. D. and Watson, A. J. M. (1996) Apoptosis and gastrointestinal pharmacology. Pharmacol. Ther. 72, 149-169
    • (1996) Pharmacol. Ther. , vol.72 , pp. 149-169
    • Pritchard, M.D.1    Watson, A.J.M.2
  • 4
    • 0033613123 scopus 로고    scopus 로고
    • Reverse biochemistry: Use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue
    • Takeuchi, T., Shuman, M. A. and Craik, C. S. (1999) Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. Proc. Natl. Acad. Sci. U.S.A. 96, 11054-11061
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11054-11061
    • Takeuchi, T.1    Shuman, M.A.2    Craik, C.S.3
  • 7
    • 0027474797 scopus 로고
    • Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells
    • Shi, Y. E., Torri, J., Yiehk, L., Wellstein, A., Lippman, M. F. and Dickson, R. B. (1993) Identification and characterization of a novel matrix-degrading protease from hormone-dependent human breast cancer cells. Cancer Res. 53, 1409-1415
    • (1993) Cancer Res. , vol.53 , pp. 1409-1415
    • Shi, Y.E.1    Torri, J.2    Yiehk, L.3    Wellstein, A.4    Lippman, M.F.5    Dickson, R.B.6
  • 8
    • 0033603574 scopus 로고    scopus 로고
    • Molecular cloning of cDNA for matriptase, a matrix degrading serine protease with trypsin-like activity
    • Lin, C. Y., Anders, J., Johnson, M., Sang, Q. A. and Dickson, R. B. (1999) Molecular cloning of cDNA for matriptase, a matrix degrading serine protease with trypsin-like activity. J. Biol. Chem. 274, 18231-18236
    • (1999) J. Biol. Chem. , vol.274 , pp. 18231-18236
    • Lin, C.Y.1    Anders, J.2    Johnson, M.3    Sang, Q.A.4    Dickson, R.B.5
  • 9
    • 0034711244 scopus 로고    scopus 로고
    • Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease
    • Lee, S.-L., Dickson, R. B. and Lin, C.-L. (2000) Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. J. Biol. Chem. 275, 36720-36725
    • (2000) J. Biol. Chem. , vol.275 , pp. 36720-36725
    • Lee, S.-L.1    Dickson, R.B.2    Lin, C.-L.3
  • 10
    • 0034714379 scopus 로고    scopus 로고
    • Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates
    • Takeuchi, T., Harris, J. L., Huang, W., Yan, K. W., Coughlin, S. R. and Craik, C. S. (2000) Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. J. Biol. Chem. 275, 26333-26342
    • (2000) J. Biol. Chem. , vol.275 , pp. 26333-26342
    • Takeuchi, T.1    Harris, J.L.2    Huang, W.3    Yan, K.W.4    Coughlin, S.R.5    Craik, C.S.6
  • 11
    • 0028349254 scopus 로고
    • Hepatocyte growth factor/scatter factor effects on epithelia. Regulation of intercellular junctions in transformed and nontransformed cell lines, basolateral polarization of c-met receptor in transformed and natural intestinal epithelia, and induction of rapid wound repair in a transformed model epithelium
    • Nusrat, A., Parkos, C. A., Bacarra, A. E., Godowski, P. J., Delp-Archer, C., Rosen, E. M. and Madara, J. L. (1994) Hepatocyte growth factor/scatter factor effects on epithelia. Regulation of intercellular junctions in transformed and nontransformed cell lines, basolateral polarization of c-met receptor in transformed and natural intestinal epithelia, and induction of rapid wound repair in a transformed model epithelium. J. Clin. Invest. 93, 2056-2065
    • (1994) J. Clin. Invest. , vol.93 , pp. 2056-2065
    • Nusrat, A.1    Parkos, C.A.2    Bacarra, A.E.3    Godowski, P.J.4    Delp-Archer, C.5    Rosen, E.M.6    Madara, J.L.7
  • 12
    • 0031743435 scopus 로고    scopus 로고
    • Urokinase and the intestinal mucosa: Evidence for a role in epithelial cell turnover
    • Gibson, P. R., Birchall, I., Rosella, O., Albert, V., Finch, C. F., Barkla, D. H. and Young, G. P. (1998) Urokinase and the intestinal mucosa: evidence for a role in epithelial cell turnover. Gut 43, 656-663
    • (1998) Gut , vol.43 , pp. 656-663
    • Gibson, P.R.1    Birchall, I.2    Rosella, O.3    Albert, V.4    Finch, C.F.5    Barkla, D.H.6    Young, G.P.7
  • 14
    • 0037161955 scopus 로고    scopus 로고
    • Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis
    • List, K., Haudenschild, C. C., Szabo, R., Chen, W., Wahl, S. M., Swaim, W., Engelholm, L. H., Behrendt, N. and Bugge, T. H. (2002) Matriptase/MT-SP1 is required for postnatal survival, epidermal barrier function, hair follicle development, and thymic homeostasis. Oncogene 21, 3765-3779
    • (2002) Oncogene , vol.21 , pp. 3765-3779
    • List, K.1    Haudenschild, C.C.2    Szabo, R.3    Chen, W.4    Wahl, S.M.5    Swaim, W.6    Engelholm, L.H.7    Behrendt, N.8    Bugge, T.H.9
  • 15
    • 0035575592 scopus 로고    scopus 로고
    • Protein trafficking in the exocytic pathway of polarized epithelial cells
    • Nelson, J. W. and Yeaman, C. (2001) Protein trafficking in the exocytic pathway of polarized epithelial cells. Trends Cell Biol. 11, 483-486
    • (2001) Trends Cell Biol. , vol.11 , pp. 483-486
    • Nelson, J.W.1    Yeaman, C.2
  • 16
    • 0037174846 scopus 로고    scopus 로고
    • Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system
    • Rosmann, S., Hahn, D., Lottaz, D., Kruse, M. N., Stocker, W. and Sterchi, E. E. (2002) Activation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating system. J. Biol. Chem. 277, 40650-40658
    • (2002) J. Biol. Chem. , vol.277 , pp. 40650-40658
    • Rosmann, S.1    Hahn, D.2    Lottaz, D.3    Kruse, M.N.4    Stocker, W.5    Sterchi, E.E.6
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-690
    • (1970) Nature (London) , vol.227 , pp. 680-690
    • Laemmli, U.K.1
  • 19
    • 0037687435 scopus 로고    scopus 로고
    • Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: A novel role of the inhibitor as an anti-granzyme a
    • Tsuzuki, S., Kokado, Y., Satomi, S., Yamasaki, Y., Hirayasu, H., Iwanaga, T. and Fushiki, T. (2003) Purification and identification of a binding protein for pancreatic secretory trypsin inhibitor: a novel role of the inhibitor as an anti-granzyme A. Biochem. J. 372, 227-233
    • (2003) Biochem. J. , vol.372 , pp. 227-233
    • Tsuzuki, S.1    Kokado, Y.2    Satomi, S.3    Yamasaki, Y.4    Hirayasu, H.5    Iwanaga, T.6    Fushiki, T.7
  • 20
    • 0029031369 scopus 로고
    • The GLUT5 hexose transporter is also localized to the basolateral membrane of the human jejunum
    • Blakemore, S. J., Aledo, J. C., James, J., Campbell, F. C., Lucocq, J. M. and Hundal, H. S. (1995) The GLUT5 hexose transporter is also localized to the basolateral membrane of the human jejunum. Biochem. J. 309, 7-12
    • (1995) Biochem. J. , vol.309 , pp. 7-12
    • Blakemore, S.J.1    Aledo, J.C.2    James, J.3    Campbell, F.C.4    Lucocq, J.M.5    Hundal, H.S.6
  • 21
    • 0028118073 scopus 로고
    • Preparation of basolateral membrane vesicles from rat enterocytes: Influence of different gradient media
    • Milovic, V., Stein, J., Ruppert, S., Zeuzem, S. and Caspary, W. F. (1994) Preparation of basolateral membrane vesicles from rat enterocytes: influence of different gradient media. Physiol. Res. 43, 75-81
    • (1994) Physiol. Res. , vol.43 , pp. 75-81
    • Milovic, V.1    Stein, J.2    Ruppert, S.3    Zeuzem, S.4    Caspary, W.F.5
  • 22
    • 0038035877 scopus 로고    scopus 로고
    • The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor
    • Oberst, M. D., Williams, C. A., Dickson, R. B., Johnson, M. D. and Lin, C. Y. (2003) The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. J. Biol. Chem. 278, 26773-26779
    • (2003) J. Biol. Chem. , vol.278 , pp. 26773-26779
    • Oberst, M.D.1    Williams, C.A.2    Dickson, R.B.3    Johnson, M.D.4    Lin, C.Y.5
  • 23
    • 0038630508 scopus 로고    scopus 로고
    • SEA (sea-urchin sperm protein, enterokinase and agrin)-module cleavage, association of fragments and membrane targeting of rat intestinal mucin Muc3
    • Khatri, I. A., Wang, R. and Forstner, J. F. (2003) SEA (sea-urchin sperm protein, enterokinase and agrin)-module cleavage, association of fragments and membrane targeting of rat intestinal mucin Muc3. Biochem. J. 372, 263-270
    • (2003) Biochem. J. , vol.372 , pp. 263-270
    • Khatri, I.A.1    Wang, R.2    Forstner, J.F.3
  • 24
    • 0028024206 scopus 로고
    • Development and hormonal modulation of postnatal expression of intestinal alkaline phosphatase mRNA species and their encoded isoenzymes
    • Yeh, K.-Y., Yeh, M., Holt, P. R. and Alpers, D. H. (1994) Development and hormonal modulation of postnatal expression of intestinal alkaline phosphatase mRNA species and their encoded isoenzymes. Biochem. J. 301, 893-899
    • (1994) Biochem. J. , vol.301 , pp. 893-899
    • Yeh, K.-Y.1    Yeh, M.2    Holt, P.R.3    Alpers, D.H.4
  • 25
    • 0024422412 scopus 로고
    • Membrane domains of intestinal epithelial cells: Distribution of Na+,K+-ATPase and the membrane skeleton in adult rat intestine during fetal development and after epithelial isolation
    • Amerongen, H. M., Mack, J. A., Wilson, J. M. and Neutra, M. R. (1989) Membrane domains of intestinal epithelial cells: distribution of Na+,K+-ATPase and the membrane skeleton in adult rat intestine during fetal development and after epithelial isolation. J. Cell Biol. 109, 2129-2138
    • (1989) J. Cell Biol. , vol.109 , pp. 2129-2138
    • Amerongen, H.M.1    Mack, J.A.2    Wilson, J.M.3    Neutra, M.R.4
  • 26
    • 0035976996 scopus 로고    scopus 로고
    • N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease
    • Cho, E.-G., Kim, M. G., Kim, C., Kim, S.-R., Seong, I. S., Chung, C., Schwartz, R. H. and Park, D. (2001) N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease. J. Biol. Chem. 276, 44581-44589
    • (2001) J. Biol. Chem. , vol.276 , pp. 44581-44589
    • Cho, E.-G.1    Kim, M.G.2    Kim, C.3    Kim, S.-R.4    Seong, I.S.5    Chung, C.6    Schwartz, R.H.7    Park, D.8
  • 27
    • 0032962252 scopus 로고    scopus 로고
    • Distribution of hepatocyte growth factor activator inhibitor type-1 (HAI-1) in human tissues: Cellular surface localization of HAI-1 in simple columnar epithelium and its modulated expression in injured and regenerative tissues
    • Kataoka, H., Suganuma, T., Shimomura, T., Itoh, H., Kitamura, N., Nabeshima, K. and Koone, M. (1999) Distribution of hepatocyte growth factor activator inhibitor type-1 (HAI-1) in human tissues: cellular surface localization of HAI-1 in simple columnar epithelium and its modulated expression in injured and regenerative tissues. J. Histochem. Cytochem. 47, 673-682
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 673-682
    • Kataoka, H.1    Suganuma, T.2    Shimomura, T.3    Itoh, H.4    Kitamura, N.5    Nabeshima, K.6    Koone, M.7
  • 28
    • 0035629458 scopus 로고    scopus 로고
    • The p85 subunit of phosphoinositide 3-kinase is associated with beta-catenin in the cadherin-based adhesion complex
    • Woodfield, R. J., Hodgkin, M. N., Akhtar, N., Morse, M. A., Fuller, K. J., Saqib, K., Thompson, N. T. and Wakelam, M. J. (2001) The p85 subunit of phosphoinositide 3-kinase is associated with beta-catenin in the cadherin-based adhesion complex. Biochem. J. 360, 335-344
    • (2001) Biochem. J. , vol.360 , pp. 335-344
    • Woodfield, R.J.1    Hodgkin, M.N.2    Akhtar, N.3    Morse, M.A.4    Fuller, K.J.5    Saqib, K.6    Thompson, N.T.7    Wakelam, M.J.8
  • 29
    • 1942486811 scopus 로고    scopus 로고
    • Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts
    • Hung, R. J., Hsu, I. W., Dreiling, J. L., Lee, M. J., Williams, C. A., Oberst, M. D., Dickson, R. B. and Lin, C. Y. (2004) Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts. Am. J. Physiol. Cell Physiol. 286, C1159-C1169
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Hung, R.J.1    Hsu, I.W.2    Dreiling, J.L.3    Lee, M.J.4    Williams, C.A.5    Oberst, M.D.6    Dickson, R.B.7    Lin, C.Y.8
  • 30
    • 0036510358 scopus 로고    scopus 로고
    • Mucin-like domain of enteropeptidase directs apical targeting in Madin-Darby canine kidney cells
    • Zheng, X. and Sadler, J. E. (2002) Mucin-like domain of enteropeptidase directs apical targeting in Madin-Darby canine kidney cells. J. Biol. Chem. 277, 6858-6863
    • (2002) J. Biol. Chem. , vol.277 , pp. 6858-6863
    • Zheng, X.1    Sadler, J.E.2
  • 31
    • 0031773999 scopus 로고    scopus 로고
    • TGN38 cycles via the basolateral membrane of polarized Caco-2 cells
    • Reaves, B. J., Roquemore, E. P., Luzio, J. P. and Banting, G. (1998) TGN38 cycles via the basolateral membrane of polarized Caco-2 cells. Mol. Membr. Biol. 15, 133-139
    • (1998) Mol. Membr. Biol. , vol.15 , pp. 133-139
    • Reaves, B.J.1    Roquemore, E.P.2    Luzio, J.P.3    Banting, G.4
  • 32
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh, M. D. (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 33
    • 0038708567 scopus 로고    scopus 로고
    • Membrane targeting of Grb2-associated binder-1 (Gab1) scaffolding protein through Src myristoylation sequence substitutes for Gab1 pleckstrin homology domain and switches an epidermal growth factor response to an invasive morphogenic program
    • Maroun, C. R., Naujokas, M. A. and Park, M. (2003) Membrane targeting of Grb2-associated binder-1 (Gab1) scaffolding protein through Src myristoylation sequence substitutes for Gab1 pleckstrin homology domain and switches an epidermal growth factor response to an invasive morphogenic program. Mol. Biol. Cell 14, 1691-1708
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1691-1708
    • Maroun, C.R.1    Naujokas, M.A.2    Park, M.3
  • 34
    • 0028258532 scopus 로고
    • Targeting of the SF/HGF receptor to the basolaterai domain of polarized epithelial cells
    • Crepaldi, T., Pollack, A. L., Prat, M., Zborek, A., Mostov, K. and Comoglio, P. M. (1994) Targeting of the SF/HGF receptor to the basolaterai domain of polarized epithelial cells. J. Cell Biol. 125, 313-320
    • (1994) J. Cell Biol. , vol.125 , pp. 313-320
    • Crepaldi, T.1    Pollack, A.L.2    Prat, M.3    Zborek, A.4    Mostov, K.5    Comoglio, P.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.